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Inside Back Cover: Flipping of a Nonproductive Substrate Binding Conformation Facilitates Hydroxynitrile Lyase Catalyzed Hydrocyanation (Angew. Chem. Int. Ed. 52/2025)

Year: 2025
Type: article
Abstract: Conformational interchange of enzyme–substrate complexes are intrinsic to catalysis, yet their transient nature makes it elusive for understanding the substrate conformational dynamics. In the Research Article (e15778) by Yi-Lei Zhao, Hui-Lei Yu, and co-workers a “flipped” substrate binding conformation in the hydroxynitrile lyase from Prunus communis (PcHNL5) is revealed. Crystallographic and computational analyses show that this non-productive state must reorganize before catalysis proceeds. Mutagenesis destabilizes this non-productive conformation, promoting conversion to the productively competent state and markedly enhancing enzymatic efficiency.
DOI: 10.1002/anie.2025-m1711061800
Authors: Yu‐Cong Zheng, Yong Mao, Qiang Geng, Fu‐Long Li, Xu‐Dong Kong, Yi‐Ke Qi, Lin Zhang, Qi Chen, Zhi‐Jun Zhang, Ran Hong, Yi‐Lei Zhao, Hui‐Lei Yu, Jian‐He Xu
Institutions: East China University of Science and Technology, State Key Laboratory of Bioreactor Engineering, Shanghai Jiao Tong University, State Key Laboratory of Microbial Metabolism, Chinese Academy of Sciences, Shanghai Institute of Organic Chemistry
Language: English
Open Access status: bronze
OpenAlex ID: W4416565653
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